Abstract
The effect of sulfated polysaccharides on the AMP-dependent activity of rabbit muscle phosphorylase b as compared with that of Na 2SO 4 has been studied. It has been shown that sulfated polysaccharides and Na 2SO 4 greatly stimulated AMP-activation of the enzyme at low AMP concentrations. Dextran sulfate and Na 2SO 4 desensitized the allosteric interactions of the enzyme towards the nucleotide activator and reversed the enzyme inhibition caused by glucose-6-phosphate and glucose. Furthermore, it was found that while dextran sulfate decreased the K m value for both substrates, glucose-1-phosphate and glycogen, sulfate anions decreased only the K m value for glycogen.
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